Helix formation in preorganized β/γ-peptide foldamers: Hydrogen-bond analogy to the α-helix without α-amino acid residues

Li Guo, Aaron M. Almeida, Weicheng Zhang, Andrew G. Reidenbach, Soo Hyuk Choi, Ilia A. Guzei, Samuel H. Gellman

Research output: Contribution to journalArticle

76 Citations (Scopus)

Abstract

We report the first high-resolution structural data for the β/γ-peptide 13-helix (i,i+3 CO⋯HN H-bonds), a secondary structure that is formed by oligomers with a 1:1 alternation of β- and γ-amino acid residues. Our characterization includes both crystallophaphic and 2D NMR data. Previous studies suggested that β/γ-peptides constructed from conformationally flexible residues adopt a different helical secondary structure in solution. Our design features preorganized β- and γ-residues, which strongly promote 13-helical folding by the 1:1 β/γ backbone.

Original languageEnglish
Pages (from-to)7868-7869
Number of pages2
JournalJournal of the American Chemical Society
Volume132
Issue number23
DOIs
Publication statusPublished - 2010 Jun 16

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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